Gideon John Davies (born 6 July 1964) FRSFRSCFMedSci is a professor of chemistry in the Structural Biology Laboratory (YSBL) at the University of York, UK.[2][7][8] Davies is best known for his ground-breaking studies into carbohydrate-active enzymes, notably analysing the conformational and mechanistic basis for catalysis and applying this for societal benefit. In 2016 Davies was appointed the Royal Society Ken Murray Research Professor at the University of York. Gideon Davies has recently been elected to the Council of the Royal Society.
Davies has won a number of awards for his work. These include The Davy Medal and Gabor Medal of the Royal Society, the John and Rita Cornforth Award (with Paul Walton[30]), the Haworth Memorial, Khorana, Peptide and Protein, Corday-Morgan and Carbohydrate Chemistry medals of the Royal Society of Chemistry, the iChemE Global Energy Award of the Institution of Chemical Engineers (with Paul Walton and Bernard Henrissat), The Whistler Prize of the International Carbohydrate Organization,[31] and the GlaxoSmithKline Award[32] of the Biochemical Society. In 2019 he was one of the members of the York Structural Biology Laboratory at the University of York that received the Queen's Anniversary Prize.
Professor Gideon Davies' research is focused on "structural enzymology". In this he addresses the enzymes, and their accessory domains, that are involved in the synthesis, modification and breakdown of carbohydrates. His chemical and structural insight into protein-carbohydrate interactions and his brilliant exploitation of advanced crystallographic methods provide the basis for understanding how the chemical and structural factors in the stereochemical pathway of the enzyme:substrate complex govern specificity and catalysis. His research is having an immense impact on carbohydrate chemistry and biology and biological catalysis generally.[33]
Gideon Davies, who is Professor of Biological Chemistry at University of York, has made world-leading contributions to Biochemistry. He has made fundamental additions to our understanding of enzyme mechanism and carbohydrate biochemistry. As a direct result of his work into the conformation of sugars during turnover, he described the rational designofhighly potent inhibitorsofO-linked glucosamine modifying enzymes. These compounds are showing potential as treatments for Alzheimer's disease. Recently he has turned to study the human microbiota, which are now recognised to be an essential component of human health, and their carbohydrate metabolism is implicated in several disease states.[34]
He was awarded the John and Rita Cornforth Award of Royal Society of Chemistry in 2020[35] and the Queen's Anniversary Prize (to YSBL) in 2019[36] He was a Haworth Memorial Lectureship of Royal Society of Chemistry in 2018[37] and a Global Energy Award of Institution of Chemical Engineers winner in 2016.[38]
^ abGloster, Tracey Maureen (2005). Transition state mimicry in glycoside hydrolysis (PhD thesis). The University of York. OCLC1063339504. EThOSuk.bl.ethos.533533.
^Henrissat, B.; Davies, G. (1997). "Structural and sequence-based classification of glycoside hydrolases". Current Opinion in Structural Biology. 7 (5): 637–44. doi:10.1016/S0959-440X(97)80072-3. PMID9345621.
^Ducros, Valérie M.-A.; Zechel, David L.; Murshudov, Garib N.; Gilbert, Harry J.; Szabó, Lóránd; Stoll, Dominik; Withers, Stephen G.; Davies, Gideon J. (2 August 2002). "Substrate distortion by a beta-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state". Angewandte Chemie International Edition in English. 41 (15): 2824–2827. doi:10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2-G. ISSN1433-7851. PMID12203498.
^Coutinho, Pedro M.; Deleury, Emeline; Davies, Gideon J.; Henrissat, Bernard (25 April 2003). "An evolving hierarchical family classification for glycosyltransferases". Journal of Molecular Biology. 328 (2): 307–317. doi:10.1016/s0022-2836(03)00307-3. ISSN0022-2836. PMID12691742.
^Yuzwa, Scott A; Macauley, Matthew S; Heinonen, Julia E; Shan, Xiaoyang; Dennis, Rebecca J; He, Yuan; Whitworth, Garrett E; Stubbs, Keith A; McEachern, Ernest J (2008). "A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo". Nature Chemical Biology. 4 (8): 483–490. doi:10.1038/nchembio.96. PMID18587388.
^Ducros, V. R.; Brzozowski, A. M.; Wilson, K. S.; Brown, S. H.; Østergaard, P.; Schneider, P.; Yaver, D. S.; Pedersen, A. H.; Davies, G. J. (1998). "Crystal structure of the type-2 Cu depleted laccase from Coprinus dnereus at 2.2 Å resolution". Nature Structural Biology. 5 (4): 310–316. doi:10.1038/nsb0498-310. PMID9546223. S2CID8642348.
